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Database: UniProt
Entry: Q8NMK7
LinkDB: Q8NMK7
Original site: Q8NMK7 
ID   SUCC_CORGL              Reviewed;         398 AA.
AC   Q8NMK7;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   29-OCT-2014, entry version 88.
DE   RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558};
DE   AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE            Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN   Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558};
GN   OrderedLocusNames=Cgl2566, cg2837;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
OS   LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00558}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAF21227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAB99959.1; -; Genomic_DNA.
DR   EMBL; BX927155; CAF21227.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_601764.2; NC_003450.3.
DR   RefSeq; WP_011265968.1; NC_006958.1.
DR   RefSeq; YP_226806.1; NC_006958.1.
DR   ProteinModelPortal; Q8NMK7; -.
DR   STRING; 196627.cg2837; -.
DR   EnsemblBacteria; BAB99959; BAB99959; BAB99959.
DR   EnsemblBacteria; CAF21227; CAF21227; cg2837.
DR   GeneID; 1020512; -.
DR   GeneID; 3345415; -.
DR   KEGG; cgb:cg2837; -.
DR   KEGG; cgl:NCgl2477; -.
DR   PATRIC; 21497168; VBICorGlu203724_2500.
DR   eggNOG; COG0045; -.
DR   KO; K01903; -.
DR   OMA; PEDAYTH; -.
DR   OrthoDB; EOG644ZT0; -.
DR   UniPathway; UPA00223; UER00999.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815; PTHR11815; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    398       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta.
FT                                /FTId=PRO_0000102829.
FT   DOMAIN        9    237       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      35    100       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       189    189       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       191    191       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   398 AA;  41764 MW;  6E0C127EC7DC5CEE CRC64;
     MDLFEYQARD LFETHGVPVL KGIVASTPEA ARKAAEEIGG LTVVKAQVKV GGRGKAGGVR
     VAPTSAQAFD AADAILGMDI KGHTVNQVMV AQGADIAEEY YFSILLDRAN RSYLAMCSVE
     GGMEIEILAK EKPEALAKVE VDPLTGIDED KAREIVTAAG FETEVAEKVI PVLIKIWQVY
     YEEEATLVEV NPLVLTDDGD VIALDGKITL DDNADFRHDN RGALAESAGG LDILELKAKK
     NDLNYVKLDG SVGIIGNGAG LVMSTLDIVA AAGERHGGQR PANFLDIGGG ASAESMAAGL
     DVILGDSQVR SVFVNVFGGI TACDVVAKGI VGALDVLGDQ ATKPLVVRLD GNNVVEGRRI
     LAEYNHPLVT VVEGMDAAAD HAAHLANLAQ HGQFATAN
//
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